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Protein

Anaphase-promoting complex subunit cut9

Gene

cut9

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. May play a pivotal role in the control of anaphase.1 Publication

GO - Biological processi

  • anaphase-promoting complex-dependent catabolic process Source: PomBase
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • positive regulation of mitotic metaphase/anaphase transition Source: PomBase

Keywordsi

Biological processCell cycle, Cell division, Mitosis, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit cut9
Alternative name(s):
20S cyclosome/APC complex protein cut9
Cell untimely torn protein 9
Gene namesi
Name:cut9
Synonyms:dre1
ORF Names:SPAC6F12.15c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC6F12.15c
PomBaseiSPAC6F12.15c cut9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi412G → D in cut9-T98; temperature-sensitive. 1 Publication1
Mutagenesisi535A → T in cut9-665; temperature-sensitive. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001062811 – 671Anaphase-promoting complex subunit cut9Add BLAST671

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41889
PaxDbiP41889
PRIDEiP41889

PTM databases

iPTMnetiP41889

Interactioni

Subunit structurei

The APC/C is composed of at least 13 subunits: apc1, apc2, nuc2, apc4, apc5, cut9, apc8, apc10, apc11, hcn1, apc13, apc14 and apc15. Homodimer. Interacts directly with nuc2 and hcn1.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi278089, 47 interactors
IntActiP41889, 6 interactors
MINTiP41889
STRINGi4896.SPAC6F12.15c.1

Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi50 – 53Combined sources4
Helixi55 – 59Combined sources5
Helixi83 – 96Combined sources14
Helixi100 – 114Combined sources15
Helixi117 – 129Combined sources13
Helixi133 – 142Combined sources10
Helixi145 – 147Combined sources3
Helixi150 – 162Combined sources13
Helixi166 – 173Combined sources8
Helixi198 – 212Combined sources15
Helixi216 – 229Combined sources14
Helixi234 – 242Combined sources9
Helixi248 – 257Combined sources10
Helixi261 – 264Combined sources4
Helixi265 – 267Combined sources3
Helixi268 – 276Combined sources9
Turni281 – 284Combined sources4
Helixi285 – 296Combined sources12
Helixi301 – 303Combined sources3
Helixi305 – 317Combined sources13
Helixi321 – 334Combined sources14
Helixi342 – 352Combined sources11
Helixi355 – 368Combined sources14
Helixi373 – 385Combined sources13
Helixi389 – 402Combined sources14
Helixi407 – 420Combined sources14
Helixi423 – 435Combined sources13
Turni436 – 439Combined sources4
Helixi442 – 454Combined sources13
Helixi457 – 470Combined sources14
Helixi475 – 487Combined sources13
Helixi491 – 507Combined sources17
Helixi513 – 515Combined sources3
Helixi516 – 528Combined sources13
Helixi532 – 545Combined sources14
Helixi550 – 562Combined sources13
Helixi566 – 579Combined sources14
Helixi584 – 592Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XPIX-ray2.60A/D1-597[»]
ProteinModelPortaliP41889
SMRiP41889
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati83 – 114TPR 1Add BLAST32
Repeati117 – 142TPR 2Add BLAST26
Repeati150 – 173TPR 3Add BLAST24
Repeati198 – 229TPR 4Add BLAST32
Repeati234 – 257TPR 5Add BLAST24
Repeati268 – 296TPR 6Add BLAST29
Repeati306 – 334TPR 7Add BLAST29
Repeati341 – 368TPR 8Add BLAST28
Repeati373 – 402TPR 9Add BLAST30
Repeati407 – 435TPR 10Add BLAST29
Repeati442 – 470TPR 11Add BLAST29
Repeati475 – 507TPR 12Add BLAST33
Repeati513 – 545TPR 13Add BLAST33
Repeati550 – 579TPR 14Add BLAST30

Domaini

TPR repeats 1-7 mediate homodimerization while TPR repeats 8 and 10-13 bind to hcn1, burying its N-terminal acetyl-methionine.1 Publication

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

HOGENOMiHOG000160791
InParanoidiP41889
KOiK03353
OMAiYIDQQQY
OrthoDBiEOG092C0SLF
PhylomeDBiP41889

Family and domain databases

Gene3Di1.25.40.10, 1 hit
InterProiView protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
PfamiView protein in Pfam
PF13181 TPR_8, 1 hit
SMARTiView protein in SMART
SM00028 TPR, 8 hits
SUPFAMiSSF48452 SSF48452, 2 hits
PROSITEiView protein in PROSITE
PS50005 TPR, 6 hits
PS50293 TPR_REGION, 2 hits

Sequencei

Sequence statusi: Complete.

P41889-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVKRTQTDS RMQSTPGNHN HPDAHANAAY MTPPSMGALN ANNSNSQLST
60 70 80 90 100
LTISPMTYLA NNTSTDGSFL KERNAQNTDS LSREDYLRLW RHDALMQQQY
110 120 130 140 150
KCAAFVGEKV LDITGNPNDA FWLAQVYCCT GDYARAKCLL TKEDLYNRSS
160 170 180 190 200
ACRYLAAFCL VKLYDWQGAL NLLGETNPFR KDEKNANKLL MQDGGIKLEA
210 220 230 240 250
SMCYLRGQVY TNLSNFDRAK ECYKEALMVD AKCYEAFDQL VSNHLLTADE
260 270 280 290 300
EWDLVLKLNY STYSKEDAAF LRSLYMLKLN KTSHEDELRR AEDYLSSING
310 320 330 340 350
LEKSSDLLLC KADTLFVRSR FIDVLAITTK ILEIDPYNLD VYPLHLASLH
360 370 380 390 400
ESGEKNKLYL ISNDLVDRHP EKAVTWLAVG IYYLCVNKIS EARRYFSKSS
410 420 430 440 450
TMDPQFGPAW IGFAHSFAIE GEHDQAISAY TTAARLFQGT HLPYLFLGMQ
460 470 480 490 500
HMQLGNILLA NEYLQSSYAL FQYDPLLLNE LGVVAFNKSD MQTAINHFQN
510 520 530 540 550
ALLLVKKTQS NEKPWAATWA NLGHAYRKLK MYDAAIDALN QGLLLSTNDA
560 570 580 590 600
NVHTAIALVY LHKKIPGLAI THLHESLAIS PNEIMASDLL KRALEENSLT
610 620 630 640 650
SGFLNSKYVF EDEVSEYMQQ SNLNTSDKSM SMEDQSGKVT ESVNDRTQVL
660 670
YADSRSEMMM DDIEGNVSEQ R
Length:671
Mass (Da):75,889
Last modified:July 15, 1998 - v2
Checksum:i5300382396270BE2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103A → C (PubMed:7798319).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31844 Genomic DNA Translation: BAA06630.1
CU329670 Genomic DNA Translation: CAB11098.1
PIRiA55164
RefSeqiNP_593301.1, NM_001018731.2

Genome annotation databases

EnsemblFungiiSPAC6F12.15c.1; SPAC6F12.15c.1:pep; SPAC6F12.15c
GeneIDi2541592
KEGGispo:SPAC6F12.15c

Similar proteinsi

Entry informationi

Entry nameiCUT9_SCHPO
AccessioniPrimary (citable) accession number: P41889
Secondary accession number(s): O14231
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 15, 1998
Last modified: April 25, 2018
This is version 143 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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